8t0i: Difference between revisions
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==Backbone Dialkylation in Peptide Hairpins: (R)-Ethylpropylglycine variant== | |||
<StructureSection load='8t0i' size='340' side='right'caption='[[8t0i]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8t0i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8T0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8T0I FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=X6E:2-ethyl-D-norvaline'>X6E</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8t0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8t0i OCA], [https://pdbe.org/8t0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8t0i RCSB], [https://www.ebi.ac.uk/pdbsum/8t0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8t0i ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Strategic incorporation of achiral C(alpha,alpha)-dialkylated amino acids with bulky substituents into peptides can be used to promote extended strand conformations and inhibit protein-protein interactions associated with amyloid formation. In this work, we evaluate the thermodynamic impact of chiral C(alpha,alpha) monomers on folding preferences in such systems through introduction of a series of C(alpha)-methylated and C(alpha)-ethylated residues into a beta-hairpin host sequence. Depending on stereochemical configuration of the artificial monomer and potential for additional hydrophobic packing, a C(alpha)-ethyl-C(alpha)-propyl glycine residue can provide similar or enhanced folded stability relative to an achiral C(alpha,alpha)-diethyl analogue. | |||
Effects of chirality and side chain length in C(alpha,alpha)-dialkylated residues on beta-hairpin peptide folded structure and stability.,Heath SL, Horne WS, Lengyel GA Org Biomol Chem. 2023 Aug 9;21(31):6320-6324. doi: 10.1039/d3ob00963g. PMID:37503895<ref>PMID:37503895</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8t0i" style="background-color:#fffaf0;"></div> | ||
[[Category: Heath | == References == | ||
[[Category: Lengyel | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus sp. 'group G']] | |||
[[Category: Heath SL]] | |||
[[Category: Horne WS]] | |||
[[Category: Lengyel GA]] | |||
Latest revision as of 08:31, 16 August 2023
Backbone Dialkylation in Peptide Hairpins: (R)-Ethylpropylglycine variant
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